Properdin System and Immunity: II. Interaction of the Properdin System with Polysaccharides

Pillemer, Louis; Schoenberg, Melvin D.; Blum, Livia; Wurz, Leona

doi:10.1126/science.122.3169.545

Cited by 226 publications

(66 citation statements)

References 29 publications

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“…Cell-wall LPS from wild-type serum-resistant Gram-negative enteric bacteria such as Salmonella is structurally and functionally composed of 3 parts: the toxic lipid A region, the common core polysaccharide, and the O antigen-specific polysaccharide (40). With regard to complement, Pillemer et al (41) originally suggested that LPS activates the properdin system, now known as the alternative pathway, without involvement of antibodies. It was later shown that the classical pathway as well as the alternative pathway is involved in complement activation by LPS, with the polysaccharide part being responsible for alternative pathway activation (42).…”

Section: Discussionmentioning

confidence: 99%

Mannan-binding lectin activates C3 and the alternative complement pathway without involvement of C2

Selander

Mårtensson

Weintraub

et al. 2007

Molecular Immunology

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Lectin pathway activation of C3 is known to involve target recognition by mannan-binding lectin (MBL)or ficolins and generation of classical pathway C3 convertase via cleavage of C4 and C2 by MBL-associated serine protease 2 (MASP-2). We investigated C3 activation in C2-deficient human sera and in sera with other defined defects of complement to assess other mechanisms through which MBL might recruit complement. The capacity of serum to support C3 deposition was examined by ELISA using microtiter plates coated with O antigen-specific oligosaccharides derived from Salmonella typhimurium, S. thompson, and S. enteritidis corresponding to serogroups B, C, and D (BO, CO, and DO). MBL bound to CO, but not to BO and DO, and efficiently supported C3 deposition in the absence of C2, C4, or MASP-2. The existence of an MBL-dependent C2 bypass mechanism for alternative pathway-mediated C3 activation was clearly demonstrated using CO, solid-phase mannan, and E. coli LPS. MASP-1 might contribute, but was not required for C3 deposition in the model used. Independent of MBL, specific antibodies to CO supported C3 deposition through classical and alternative pathways. MBL-dependent C2 bypass activation could be particularly important in various inherited and acquired complement deficiency states.

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Section: Discussionmentioning

confidence: 99%

Mannan-binding lectin activates C3 and the alternative complement pathway without involvement of C2

Selander

Mårtensson

Weintraub

et al. 2007

Molecular Immunology

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“…This was found to be due to the property of R lipopolysaccharides to reaggregate into a large-molecular-weight form through absorption of Mg2+ and Ca2+ present in the guinea pig serum used as complement source. Defective lipopolysaccharides derived from the Ra and Rb classes showed only negligible anti-complementary activity which did not increase by conversion into salt forms with high molecular weight.Many lipopolysaccharides interact with complement in vitro leading to loss of complement hemolytic activity [1,2]. This property is embedded in the lipid A part of the molecule and is expressed only by soluble lipopolysaccharides [ 2 ] .…”

mentioning

confidence: 99%

“…Many lipopolysaccharides interact with complement in vitro leading to loss of complement hemolytic activity [1,2]. This property is embedded in the lipid A part of the molecule and is expressed only by soluble lipopolysaccharides [ 2 ] .…”

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confidence: 99%

The Role of the Physical State of Lipopolysaccharides in the Interaction with Complement

Galanos

Lüderitz

1976

European Journal of Biochemistry

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Lipopolysaccharides interact with complement onIy when they are present in a state of high aggregation with a high apparent molecular weight. Lipopolysaccharides in uniform salt forms prepared by electrodialysis and neutralization with different bases exhibited distinct differences in their anticomplementary activity which correlated with differences in their sedimentation coefficients.Conversion of smooth (S) form lipopolysaccharides into the low-molecular-weight triethylamine form completely abolished their anti-complementary activity while conversion into the highmolecular-weight sodium form increased their activity. In contrast, a similar treatment of highly defective Re and Rd rough (R) form lipopolysaccharides had no effect on their ability to interact with complement. Both the triethylamine and sodium forms were strongly anti-complementary despite large differences in their molecular weight. This was found to be due to the property of R lipopolysaccharides to reaggregate into a large-molecular-weight form through absorption of Mg2+ and Ca2+ present in the guinea pig serum used as complement source. Defective lipopolysaccharides derived from the Ra and Rb classes showed only negligible anti-complementary activity which did not increase by conversion into salt forms with high molecular weight.Many lipopolysaccharides interact with complement in vitro leading to loss of complement hemolytic activity [1,2]. This property is embedded in the lipid A part of the molecule and is expressed only by soluble lipopolysaccharides [ 2 ] . In the last years, much effort has been devoted to identifying the mechanisms underlying this interaction and much information has become available. Thus, it is known today that interaction of lipopolysaccharides with complement involves mainly the terminal complement compo-. nents, and that serum factors other than classical antibody are required [3 -51.Although lipid A is a common constituent of all lipopolysaccharides, a number of preparations exists which although soluble, do not exhibit this activity [2,6]. The inability of many lipopolysaccharides to interact with complement has drawn little attention and consequently structural or physicochemical requirements that may be prerequisite for the expression of anti-complementary activity by lipopolysaccharides have remained virtually unexplored.Lipopolysaccharides are acidic macromolecules due to the presence of phosphate, pyrophosphate and carboxyl groups in the molecule.Recently we have shown that the physical state of a lipopolysaccharide is determined by the type of basic ions that are present in salt form with acidic groups in the molecule. With the aid of electrodialysis it was possible to obtain lipopolysaccharides in defined salt forms which showed distinct differences in their molecular weight as judged by sedimentation coefficient determinations in the ultracentrifuge [7].In the present communication lipopolysaccharides in defined salt forms are employed to find out whether a relation exists between the molecular size of a ...

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“…Pillemer et al (1955) demonstrated that the essential activity of zymosan consists in a glucan-rich fraction. In contrast, the mannan-rich fraction-glucomannan proteinshowed little activity.…”

Section: Introductionmentioning

confidence: 99%

β-Glucan in Allergies

Šíma¹,

Větvička²

2017

American Journal of Immunology

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Multiple effects of β-glucan are well established. Together with the effects on antibacterial and anticancer immunity, glucan has been shown to stimulate bone marrow cells, lower cholesterol and to protects against stress and some kinds of poisoning. However, despite literally thousands of papers describing biological effects of β-glucan, only limited attention has been focused on the role of β-glucan in allergic reactions. Our review is focused on evaluating the current knowledge of the possible role of β-glucan in allergic reactions. Most of published studies concur that based on the improved Th1/Th2 balance, β-glucan showed a potential for development as an adjunct to the standard treatment of in patients with allergies.

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Properdin System and Immunity: II. Interaction of the Properdin System with Polysaccharides

Cited by 226 publications

References 29 publications

Mannan-binding lectin activates C3 and the alternative complement pathway without involvement of C2

Mannan-binding lectin activates C3 and the alternative complement pathway without involvement of C2

The Role of the Physical State of Lipopolysaccharides in the Interaction with Complement

β-Glucan in Allergies

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Properdin System and Immunity: II. Interaction of the Properdin System with Polysaccharides

Cited by 226 publications

References 29 publications

Mannan-binding lectin activates C3 and the alternative complement pathway without involvement of C2

Mannan-binding lectin activates C3 and the alternative complement pathway without involvement of C2

The Role of the Physical State of Lipopolysaccharides in the Interaction with Complement

&beta;-Glucan in Allergies

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β-Glucan in Allergies